ID A0A1Q4U6H2_9MYCO Unreviewed; 87 AA.
AC A0A1Q4U6H2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 05-JUL-2017, entry version 4.
DE RecName: Full=ATP synthase subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
DE AltName: Full=ATP synthase F(0) sector subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
DE AltName: Full=F-type ATPase subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
DE Short=F-ATPase subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
DE AltName: Full=Lipid-binding protein {ECO:0000256|HAMAP-Rule:MF_01396};
GN Name=atpE {ECO:0000256|HAMAP-Rule:MF_01396};
GN ORFNames=EB75_17890 {ECO:0000313|EMBL:OKH81190.1};
OS Mycobacterium sp. ST-F2.
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1490484 {ECO:0000313|EMBL:OKH81190.1, ECO:0000313|Proteomes:UP000186514};
RN [1] {ECO:0000313|EMBL:OKH81190.1, ECO:0000313|Proteomes:UP000186514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST-F2 {ECO:0000313|EMBL:OKH81190.1,
RC ECO:0000313|Proteomes:UP000186514};
RA Guo F., Zhang T.;
RT "Mycobacterial species and functional characteristics in global
RT wastewater treatment plants.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the
CC presence of a proton or sodium gradient. F-type ATPases consist of
CC two structural domains, F(1) containing the extramembraneous
CC catalytic core and F(0) containing the membrane proton channel,
CC linked together by a central stalk and a peripheral stalk. During
CC catalysis, ATP synthesis in the catalytic domain of F(1) is
CC coupled via a rotary mechanism of the central stalk subunits to
CC proton translocation. {ECO:0000256|HAMAP-Rule:MF_01396}.
CC -!- FUNCTION: Key component of the F(0) channel; it plays a direct
CC role in translocation across the membrane. A homomeric c-ring of
CC between 10-14 subunits forms the central stalk rotor element with
CC the F(1) delta and epsilon subunits. {ECO:0000256|HAMAP-
CC Rule:MF_01396}.
CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic
CC core - and F(0) - the membrane proton channel. F(1) has five
CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0)
CC has three main subunits: a(1), b(2) and c(10-14). The alpha and
CC beta chains form an alternating ring which encloses part of the
CC gamma chain. F(1) is attached to F(0) by a central stalk formed by
CC the gamma and epsilon chains, while a peripheral stalk is formed
CC by the delta and b chains. {ECO:0000256|SAAS:SAAS00732135}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC Rule:MF_01396}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01396}.
CC -!- SIMILARITY: Belongs to the ATPase C chain family.
CC {ECO:0000256|HAMAP-Rule:MF_01396}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01396}.
CC -!- CAUTION: The sequence shown here is derived from an
CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC preliminary data. {ECO:0000313|EMBL:OKH81190.1}.
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DR EMBL; JMHT01000054; OKH81190.1; -; Genomic_DNA.
DR RefSeq; WP_020104130.1; NZ_JMHT01000054.1.
DR GeneID; 32358922; -.
DR Proteomes; UP000186514; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP.
DR Gene3D; 1.20.20.10; -; 1.
DR HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR InterPro; IPR005953; ATP_synth_csu_bac/chlpt.
DR InterPro; IPR000454; ATP_synth_F0_csu.
DR InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR PANTHER; PTHR10031; PTHR10031; 1.
DR Pfam; PF00137; ATP-synt_C; 1.
DR PRINTS; PR00124; ATPASEC.
DR SUPFAM; SSF81333; SSF81333; 1.
DR TIGRFAMs; TIGR01260; ATP_synt_c; 1.
DR PROSITE; PS00605; ATPASE_C; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01396};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01396,
KW ECO:0000256|SAAS:SAAS00732129};
KW CF(0) {ECO:0000256|HAMAP-Rule:MF_01396};
KW Complete proteome {ECO:0000313|Proteomes:UP000186514};
KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01396};
KW Hydrolase {ECO:0000313|EMBL:OKH81190.1};
KW Ion transport {ECO:0000256|HAMAP-Rule:MF_01396};
KW Lipid-binding {ECO:0000256|HAMAP-Rule:MF_01396};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01396};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01396};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01396};
KW Transport {ECO:0000256|HAMAP-Rule:MF_01396}.
FT TRANSMEM 54 82 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_01396}.
FT DOMAIN 16 75 ATP-synt_C. {ECO:0000259|Pfam:PF00137}.
FT SITE 66 66 Reversibly protonated during proton
FT transport. {ECO:0000256|HAMAP-Rule:
FT MF_01396}.
SQ SEQUENCE 87 AA; 8615 MW; 4703D5CC92093256 CRC64;
MADAATNATI IQGALIGGGL IMAGGAIGAG IGDGIAGNAL ISGIARQPEA QGRLFTPFFI
TVGLVEAAYF INLAFMALFV FATPGLS
//